Mycobacterium tuberculosis (Mtb) is the causative agent behind the deadly disease tuberculosis and is the single most infectious agent. Current drug treatment for Mtb infection is hindered partly due to patient noncompliance and the emergence of antibiotic-resistant strains. Mtb known to enter a latent state and can activate in immunocompromised individuals, such as those with HIV/AIDS. As it is imperative to identify potential Mtb drug targets, a promising area of Mtb research involves investigating Mtb’s central metabolism which allows the pathogen to survive by scavenging a broad range of host derived nutrients. There is an even greater appeal to investigate the interface of Mtb metabolism and virulence and to further identify novel Mtb drug targets. Here we present the identification of a novel histidine kinase system, which has been demonstrated as essential for Mtb survival in human macrophages and necessary for sustaining infection in mice. We propose that the novel virulence associated dikinase, (VadK) can alter Mtb virulence through its interaction with its predicted protein partner, the putative transcriptional regulator Rv1126c. I will test this hypothesis using biochemical and structural techniques to characterize VadK kinase activity and its interaction with Rv1126c. Biochemical characterization of VadK suggests that it is able to autophosphorylate using ATP and the divalent metal ion Mg2+ as its ligands. We will determine if Mg2+ is the only divalent metal that catalyzes this reaction. We also demonstrate that VadK is able to phosphoryl transfer to Rv1126c, suggestive of a protein-protein interaction. Results of this study will provide insight into the mechanism of action of this potential drug target and further aid in the development of novel therapeutics through structure-based inhibitor design.